Premium
The importance of C‐terminal amino acid residues of actin to the inhibition of actomyosin ATPase activity by caldesmon and troponin I
Author(s) -
Makuch Robert,
Kołakowski Janusz,
Dąbrowska Renata
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80546-s
Subject(s) - caldesmon , actin , biochemistry , chemistry , troponin , atpase , tropomyosin , troponin c , actina , troponin i , amino acid residue , amino acid , biophysics , calmodulin , peptide sequence , biology , enzyme , cytoskeleton , medicine , myocardial infarction , gene , cell
Proteolytic elimination of three C‐terminal amino acid residues from actin weakens its interaction with caldesmon and troponin I and, in consequence, lowers the inhibitory effects of both proteins on actomyosin ATPase activity. These results prove the importance of C‐terminal extremity of actin to the overall interaction of this protein with caldesmon and troponin I.